Yes / Incoherent neutron spectroscopy, in combination with dynamic light scattering, was used to investigate the effect of ligand binding on the center-of-mass self-diffusion and internal diffusive dynamics of Escherichia coli aspartate α-decarboxylase (ADC). The X-ray crystal structure of ADC in complex with the D-serine inhibitor was also determined, and molecular dynamics simulations were used to further probe the structural rearrangements that occur as a result of ligand binding. These experiments reveal that D-serine forms hydrogen bonds with some of the active site residues, that higher order oligomers of the ADC tetramer exist on ns–ms time-scales, and also show that ligand binding both affects the ADC internal diffusive dynamics and appears to further increase the size of the higher order oligomers. / TR acknowledges a PhD studentship jointly funded by the ILL and the Universität Hamburg (Federal Excellence Cluster Hamburg Centre for Ultrafast Imaging EXC 1074).
| Identifer | oai:union.ndltd.org:BRADFORD/oai:bradscholars.brad.ac.uk:10454/19983 |
| Date | 30 August 2024 |
| Creators | Raskar, T., Niebling, S., Devos, J.M., Yorke, Briony A., Hartlein, M., Huse, N., Forsyth, V.T., Seydel, T., Pearson, A.R. |
| Source Sets | Bradford Scholars |
| Language | English, English |
| Detected Language | English |
| Type | Article, Published version |
| Rights | This article is licensed under a Creative Commons Attribution 3.0 Unported Licence., CC-BY |
Page generated in 0.0014 seconds